White clover (Trifolium repens L.) plants were grown in either P-containing
liquid media, or in media with the sole source of phosphate removed (P-dep
rived). At 29 d, plants were harvested and a water-soluble whole tissue ext
ract and an ionically-bound (1 M salt-extractable) cell wall protein extrac
t made from root and leaf tissue. Acid phosphatase activity was highest in
all extracts from root and leaf tissue excised from P-deprived plants, with
the biggest difference (4.5-fold) in root cell walls. The smallest fold-in
crease was observed in the leaf water-soluble extract. The relative intensi
ty of several, although not all, acid phosphatase isoenzymes was also highe
st in extracts from P-deprived plants. Up to the limits of detection used,
no new acid phosphatase isoenzymes could be detected in extracts from plant
s maintained either in P-deprived or P-containing media. The complement of
ionically-bound (1 M salt-extractable) cell wall glycoproteins in leaf and
root tissue extracts maintained in P-deprived and P-containing media was al
so compared. Using SDS-PAGE and immune-recognition with mAb 2.23, a monoclo
nal antibody that specifically recognises xylose/fucose mixed-type N-linked
glycans, glycoproteins of 30 and 31 kDa were identified which were more pr
evalent in the P-deprived root cell wall. Further, a protein of 60 kDa was
identified, which was prevalent in root cell wall extracts from plants main
tained in P-containing media. The GNA lectin, which detects oligomannose N-
linked structures, identified a glycoprotein of 37 kDa which was more preva
lent in the P-deprived root cell wall. (C) Elsevier, Paris.